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来自Xanthomonas orzyae的Hpa1蛋白的生物物理特征

Jaimini Patoliya¹, Khushali Thaker¹, Jahanvi Bajpai¹

¹Department of Biochemistry and Forensic Sciences, University School of Sciences, Gujarat University, Ahmedabad 380009, India.

Biochimica et biophysica acta. Proteins and proteomics

|November 9, 2025

概括

来自Xanthomonas oryzae pv. 的哈尔蛋白 Hpa1 oryzae (Xoo) 作为一种没有酶活性的生物刺激剂. 它的本土形状对于功能来说并不必不可少,这表明了农业应用的潜力.

科学领域:

植物病理学植物病理学
分子生物学分子生物学
生物化学生物化学

背景情况:

克桑托莫纳斯里扎 (Xanthomonas oryzae pv.) 是一个植物. 桃菌 (Xoo) 导致大米中的细菌病变,通过III型分泌系统 (T3SS) 分泌效应剂.
哈尔蛋白 Hpa1 是一个调节植物免疫力的T3SS效应体,并充当生物刺激剂,促进生长和防御.
与许多T3SS效应剂不同,Hpa1缺乏酶活性.

研究的目的:

克隆,表达和净化来自Xoo BXO1菌株的 hpa1基因.
描述重组Hpa1蛋白的生物物理特性和稳定性.
研究Hpa1形状与其生物功能之间的关系.

主要方法:

在大肠杆菌罗塞塔细胞中基因克隆和表达.
使用Ni-NTA染色学净化蛋白质.
在SDS-PAGE,西部斑点,MALDI-TOF,CD光谱,ANS光和热转移测试中.
评估Nicotiana benthamiana的HR诱导活动.

主要成果:

再组合的Hpa1蛋白 (∼16.5kDa) 已经成功净化.
生物物理特征揭示了具有中等稳定性的主要α螺旋结构.
在pH 5时,Hpa1表现出最佳的结构保留和与TFE相关的度依赖的α-螺旋增强.
热稳定性测试证实,Hpa1功能不需要原生形状.

结论:

这项研究成功地特征了重组Hpa1蛋白.
Hpa1显示出作为一种以蛋白质为基础的农业生物刺激剂的潜力.
Hpa1作为研究内在无序但功能稳定的蛋白质的模型.

关键词:

一个圆形的二重化.光光谱学是一种光谱学.哈尔哈尔哈尔哈尔哈尔热稳定蛋白质是一种热稳定蛋白质.蛋白质的展开蛋白质的展开热转移检测试验热转移检测试验热稳定性热稳定性

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